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Database: UniProt
Entry: F0KJ37_ACICP
LinkDB: F0KJ37_ACICP
Original site: F0KJ37_ACICP 
ID   F0KJ37_ACICP            Unreviewed;       299 AA.
AC   F0KJ37;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=8-oxo-dGTP diphosphatase {ECO:0000256|ARBA:ARBA00040794};
DE            EC=3.6.1.55 {ECO:0000256|ARBA:ARBA00038905};
DE   AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase {ECO:0000256|ARBA:ARBA00042798};
DE   AltName: Full=Mutator protein MutT {ECO:0000256|ARBA:ARBA00041979};
DE   AltName: Full=dGTP pyrophosphohydrolase {ECO:0000256|ARBA:ARBA00041592};
GN   OrderedLocusNames=BDGL_001778 {ECO:0000313|EMBL:ADY82364.1};
OS   Acinetobacter calcoaceticus (strain PHEA-2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY82364.1, ECO:0000313|Proteomes:UP000007477};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PHEA-2;
RA   Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT   "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT   Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT   environmental adaptation.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY82364.1, ECO:0000313|Proteomes:UP000007477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY82364.1,
RC   ECO:0000313|Proteomes:UP000007477};
RX   PubMed=21441526; DOI=10.1128/JB.00261-11;
RA   Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA   Yuan M., Zhou Z., Elmerich C., Lin M.;
RT   "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT   industry wastewater.";
RL   J. Bacteriol. 193:2672-2673(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-GTP + H2O = 8-oxo-GMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:67616, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:143553, ChEBI:CHEBI:145694;
CC         Evidence={ECO:0000256|ARBA:ARBA00036904};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55;
CC         Evidence={ECO:0000256|ARBA:ARBA00035861};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582}.
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DR   EMBL; CP002177; ADY82364.1; -; Genomic_DNA.
DR   RefSeq; WP_014207219.1; NC_016603.1.
DR   RefSeq; YP_004996046.1; NC_016603.1.
DR   AlphaFoldDB; F0KJ37; -.
DR   STRING; 871585.BDGL_001778; -.
DR   GeneID; 11639965; -.
DR   KEGG; acc:BDGL_001778; -.
DR   PATRIC; fig|871585.3.peg.1773; -.
DR   eggNOG; COG0352; Bacteria.
DR   eggNOG; COG1051; Bacteria.
DR   HOGENOM; CLU_076087_0_0_6; -.
DR   OrthoDB; 9810648at2; -.
DR   Proteomes; UP000007477; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd03425; MutT_pyrophosphohydrolase; 1.
DR   CDD; cd00564; TMP_TenI; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR047127; MutT-like.
DR   InterPro; IPR029119; MutY_C.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR036206; ThiamineP_synth_sf.
DR   InterPro; IPR022998; ThiamineP_synth_TenI.
DR   PANTHER; PTHR47707; 8-OXO-DGTP DIPHOSPHATASE; 1.
DR   PANTHER; PTHR47707:SF1; NUDIX HYDROLASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14815; NUDIX_4; 1.
DR   Pfam; PF02581; TMP-TENI; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Mutator protein {ECO:0000256|ARBA:ARBA00022457};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007477};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT   DOMAIN          4..128
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   299 AA;  34282 MW;  839EFDE13C857B8A CRC64;
     MLKPIVDVAI AILIHRGKIL VGWREEQQHQ GGKHEFPGGK VEQGETPEEA CRREIYEEVG
     IGLKDWHQFD YIHHEYDDII VNLHLFHSYV PDELLNLIHQ PWAWYTREQL LHLNFPKANK
     DIIKRLYWPH LIKISNTLSM VESSEALLYW RIENEAEQQY IEQLTALDEG QRSSLIINVD
     IWWQLSPELQ KQIKTVHLKQ SQLMNLHKGD LTVGVRYIAA CHDAVSLKQA QQIGCDAVFI
     SPVKSTTTHP EAVALGWERF SDLAQNSQIP VFALGGVHPD DLATAQQHGA YGLAGIRNF
//
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